Steroidal compounds related to PROGESTERONE, the major mammalian progestational hormone. Progesterone congeners include important progesterone precursors in the biosynthetic pathways, metabolites, derivatives, and synthetic steroids with progestational activities.

A heterogeneous family of water-soluble structural proteins found in cells of the vertebrate lens. The presence of these proteins accounts for the transparency of the lens. The family is composed of four major groups, alpha, beta, gamma, and delta, and several minor groups, which are classed on the basis of size, charge, immunological properties, and vertebrate source. Alpha, beta, and delta crystallins occur in avian and reptilian lenses, while alpha, beta, and gamma crystallins occur in all other lenses.

The basic subunit of beta-crystallins.

The acidic subunit of beta-crystallins.

A transparent, biconvex structure of the EYE, enclosed in a capsule and situated behind the IRIS and in front of the vitreous humor (VITREOUS BODY). It is slightly overlapped at its margin by the ciliary processes. Adaptation by the CILIARY BODY is crucial for OCULAR ACCOMMODATION.

A subclass of crystallins that found in the lens (LENS, CRYSTALLINE) of VERTEBRATES. Gamma-crystallins are similar in structure to BETA-CRYSTALLINS in that they both form into a Greek key-like structure. They are composed of monomeric subunits.

A class of crystallins that provides refractive power and translucency to the lens (LENS, CRYSTALLINE) in VERTEBRATES. Beta-crystallins are similar in structure to GAMMA-CRYSTALLINS in that they both contain Greek key motifs. Beta-crystallins exist as oligomers formed from acidic (BETA-CRYSTALLIN A CHAIN) and basic (BETA-CRYSTALLIN B CHAIN) subunits.

A protein phytotoxin from the seeds of Ricinus communis, the castor oil plant. It agglutinates cells, is proteolytic, and causes lethal inflammation and hemorrhage if taken internally.

One of the subunits of alpha-crystallins. Unlike ALPHA-CRYSTALLIN B CHAIN the expression of ALPHA-CRYSTALLIN A CHAIN is limited primarily to the lens (LENS, CRYSTALLINE).

A subclass of crystallins that provides the majority of refractive power and translucency to the lens (LENS, CRYSTALLINE) in VERTEBRATES. Alpha-crystallins also act as molecular chaperones that bind to denatured proteins, keep them in solution and thereby maintain the translucency of the lens. The proteins exist as large oligomers that are formed from ALPHA-CRYSTALLIN A CHAIN and ALPHA-CRYSTALLIN B CHAIN subunits.

One of the alpha crystallin subunits. In addition to being expressed in the lens (LENS, CRYSTALLINE), alpha-crystallin B chain has been found in a variety of tissues such as HEART; BRAIN; MUSCLE; and KIDNEY. Accumulation of the protein in the brain is associated with NEURODEGENERATIVE DISEASES such as CREUTZFELDT-JAKOB SYNDROME and ALEXANDER DISEASE.

A subclass of crystallins found in the lens (LENS, CRYSTALLINE) in BIRDS and REPTILES. They are inactive forms of the enzyme argininosuccinate lyase.

Partial or complete opacity on or in the lens or capsule of one or both eyes, impairing vision or causing blindness. The many kinds of cataract are classified by their morphology (size, shape, location) or etiology (cause and time of occurrence). (Dorland, 27th ed)

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

A toxic lectin from the seeds of jequirity, Abrus precatorius L. Very active poison. Five different proteins have so far been isolated: Abrus agglutinin, the component responsible for: hemagglutinating activity, & abrins a-d, the toxic principals each consisting of two peptide chains are held together by disulfide bonds.

A genus of poisonous snakes of the subfamily Elapinae of the family ELAPIDAE. They comprise the kraits. Twelve species are recognized and all inhabit southeast Asia. They are considered extremely dangerous. (Moore: Poisonous Snakes of the World, 1980, p120)

An interleukin-1 subtype that is synthesized as an inactive membrane-bound pro-protein. Proteolytic processing of the precursor form by CASPASE 1 results in release of the active form of interleukin-1beta from the membrane.

In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

An 11-kDa protein associated with the outer membrane of many cells including lymphocytes. It is the small subunit of the MHC class I molecule. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2-microglobulin is present in small amounts in serum, csf, and urine of normal people, and to a much greater degree in the urine and plasma of patients with tubular proteinemia, renal failure, or kidney transplants.